I meant to, to study chemistry, and it was really intended by my family that, whatever happened, I should go to Oxford, which was where my father had been before me, because sadly he had no boys, so I was the best he could do... to manage.

[Q] Now, where there any difficulties in getting into Oxford from that school, I can imagine some?

Yes, then we decided to... after I'd taken school certificate and got exemption from London, matriculation for the subjects we took, we went over to Oxford, to the staff at Somerville, to ask what I had to do to do chemistry, and we found I wasn't qualified to come to Oxford at all, because, at that time, I had to have done Latin, which I had not done, and a second science, which I had not done; so I spent a year getting these extra qualifications before I tried the college scholarship exam.

[Q] But that went all right?

That went, that went all right. As, as my very, very old science tutor at Somerville said, my knowledge of the second science was a bit weak.

[Q] That was presumably physics, was it?

No, it wasn't. That was the awful thing. It should have been physics, according to the fine print of the register for the examination regulations. It was in fact botany, because botany I could get a certain amount of help with from a friend of my mother's who lived near us. So there it was.

British pioneer of X-ray crystallography, Dorothy Hodgkin (1910-1994), is best known for her ground-breaking discovery of the structures of penicillin, insulin and vitamin B12. At age 18, she started studying chemistry at Somerville College, Oxford, then one of the University of Oxford colleges for women only. She also studied at the University of Cambridge under John Desmond Bernal, where she became aware of the potential of X-ray crystallography to determine the structure of proteins. Together with Sydney Brenner, Jack Dunitz, Leslie Orgel, and Beryl Oughton, she was one of the first people in April 1953 to see the model of the structure of DNA, constructed by Francis Crick and James Watson. She was awarded the 1964 Nobel Prize in Chemistry and is also known for her peace work with organisations such as Science for Peace and the Medical Aid Committee for Vietnam. All recorded material copyright of The Biochemical Society.

Guy Dodson studied chemistry and physical science at the University of New Zealand, followed by a PhD on the crystallographic study of an alkaloid. In 1961, he came to Oxford to work on the crystal structure of insulin. In the mid 1970s Guy and his wife moved to York University to establish a laboratory. In addition to insulin studies the laboratory has investigated many complex molecules of medical significance, including haemoglobin, myoglobin, HIV related proteins, proteases and proteins involved in managing nucleic acids in cells. In 1993, he went to the NIMR in London to establish a crystallographic group in an environment that spanned molecular, physiological and disease-related disciplines. Here his research began on some cell signalling proteins. His interests on medically relevant proteins included prions, malarial and TB proteins, and some clinically relevant thrombin inhibitors. Guy Dodson retired in 2004 but is still finding much to do in York and the NIMR.